Production of S-Methyl Thioacetate from Methyl Mercaptan by Saccharomyces cerevisiae |
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Authors: | Shin-Ichi Matsui Seizo Yabuuchi Mikio Amaha |
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Affiliation: | Central Research Laboratories, Asahi Breweries, Ltd., Ohmori-kita, Ohta-ku, Tokyo 143, Japan |
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Abstract: | Physicochemical properties of human к-casein were studied by ultracentrifugal analysis and circular dichroism (CD) measurement. The result of sedimentation velocity analysis in 50mm imidazole-HCl buffer at pH 7.0 showed that human к-casein was present in a monomerie form with S°20.w of 2.7S. The molecular weight of this protein was estimated to be 38,000 by a short column method. The molecular shape was considered to be a flat ellipsoid with the shape factor of 16.74 and with the frictional coefficient of 2.17. From the result of CD measurement, human к-casein was computed to have 2% α-helix, 43% α-sheet and 26% α-turn structures. Interaction of human к-casein with human к-casein was observed by sedimentation velocity analysis and discpolyacrylamide gel electrophoresis, but no association occurred between human к-casein and human lactoferrin under the conditions we studied. |
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